Journal of fish pathology (한국어병학회지)

The Korean Society of Fish Pathology (한국어병학회)
권호 표지
DOI QR코드

DOI QR Code

Isoform-specific response of two GAPDH paralogs during bacterial challenge and metal exposure in mud loach (Misgurnus mizolepis: Cypriniformes) kidney and spleen

  • Cho, Young-Sun (Institute of Marine Living Modified Organisms, Pukyong National University) ;
  • Kim, Dong-Soo (Institute of Marine Living Modified Organisms, Pukyong National University) ;
  • Nam, Yoon-Kwon (Institute of Marine Living Modified Organisms, Pukyong National University)
  • Received : 2011.09.07
  • Accepted : 2011.11.19
  • Published : 2011.12.31
Download PDF
⟨ Previous Next ⟩

Abstract

Gene expression of two glyceraldehyde-3-phosphate dehydrogenase (GAPDH) paralogs was examined during Edwardsiella tarda challenge and heavy metal exposures in mud loach (Misgurnus mizolepis; Cypriniformes) kidney and spleen. Transcription of the two mud loach GAPDH paralogs (mlGAPDH-1 and mlGAPDH-2) was significantly modulated by these stimulatory challenges in an isoform-dependent manner. Based on the real-time RT-PCR analysis, the mlGAPDH-2 transcripts were more preferentially induced by E. tarda challenge, whereas the mlGAPDH-1 transcripts were proven to show more inducibility in response to heavy metal exposure using Cd, Cu, Mn and Zn at $5{\mu}M$. Their isoform-specific response patterns were closely in accordance with the TF binding profiles in promoter and intron-1 of the two mlGAPDH isoforms, in which the mlGAPDH-2 has more binding sites for immune-related transcription factors than mlGAPDH-1 while the mlGAPDH-1 possesses exclusively metal responsive elements in its intron. Collectively, the mlGAPDHs are potentially involved in cellular pathways independent of glycolysis and the two GAPDH paralogs might undergo functional diversification or subfunctionalization at least at the transcription level.

Keywords

References

  1. Andrews, G.K.: Regulation of metallothionein gene expression by oxidative stress and metal irons. Biochem. Pharmacol., 59:95-104, 2000. https://doi.org/10.1016/S0006-2952(99)00301-9
  2. Azam, S., Jouvet, N., Jilani, A., Vongsamphanh, R., Yang, X., Yang, S. and Ramotar, D.: Human glyceraldehyde-3-phosphate dehydrogenase plays a direct role in reactivating oxidized forms of the DNA repair enzyme APE1. J. Biol. Chem., 283:30632-30641, 2008. https://doi.org/10.1074/jbc.M801401200
  3. Bannerman, D.D. and Goldblum, S.E.: Mechanisms of bacterial lipopolysaccharide-induced endothelial apoptosis. Am. J. Physiol. Lung Cell Mol. Physiol., 284:L899-L914, 2003.
  4. Bols, N.C., Brubacher, J.L., Ganassin, R.C. and Lee, L.E.J.: Ecotoxicology and innate immunity in fish. Dev. Comp. Immunol., 25:853-873, 2001. https://doi.org/10.1016/S0145-305X(01)00040-4
  5. Booth, N.J. and Bilodeau-Bourgeois, A.L.: Proteomic analysis of head kidney tissue from high and low susceptibility families of channel catfish following challenge with Edwardsiella ictaluri. Fish Shellfish Immunol., 26:193-196, 2009. https://doi.org/10.1016/j.fsi.2008.03.003
  6. Cho, Y.S., Lee, S.Y., Kim, K.H. and Nam, Y.K.: Differential modulations of two glyceraldehyde 3-phosphate dehydrogenase mRNAs in response to bacterial and viral challenges in a marine teleost Oplegnathus fasciatus (Perciformes). Fish Shellfish Immunol., 25:472-476, 2008. https://doi.org/10.1016/j.fsi.2008.07.007
  7. Cho, Y.S., Lee, S.Y., Kim, K.Y. and Nam, Y.K.: Two metallothionein genes from mud loach Misgurnus mizolepis (Teleostei; Cypriniformes): Gene structure, genomic organization, and mRNA expression analysis. Comp. Biochem. Physiol., 153B:317-326, 2009.
  8. Dang, W. and Sun, L.: Determination of internal controls for quantitative real time RT-PCR analysis of the effect of Edwardsiella tarda infection on gene expression in turbot (Scophthalmus maximus). Fish Shellfish Immunol., 30:720-728, 2011. https://doi.org/10.1016/j.fsi.2010.12.028
  9. Demarse, N.A., Ponnusamy, S., Spicer, E.K., Apohan, E., Baatz, J.E., Ogretmen, B. and Davies, C.: Direct binding of glyceraldehyde 3-phosphate dehydrogenase to telomeric DNA protects telomeres against chemotherapy-induced rapid degradation. J. Mol. Biol., 394:789-803, 2009. https://doi.org/10.1016/j.jmb.2009.09.062
  10. Ishitani, R., Tajima, H., Takata, H., Tsuchiya, K., Kuwae, T., Yamada, M., Takahashi, H., Tatton, N.A. and Katsube, N.: Proapoptotic protein glyceraldehyde-3- phosphate dehydrogenase: a possible site of action of antiapoptotic drugs. Prog. Neuro-Psychopharmacol. Biol. Psychiatry, 27:291-301, 2003. https://doi.org/10.1016/S0278-5846(03)00024-1
  11. Kim, K.Y. and Nam, Y.K.: Evolutionary history of two paralogous glyceraldehyde 3-phosphate dehydrogenase genes in teleosts. J. Fish. Sci. Technol., 11:177-181, 2008.
  12. Lee, S.Y., Stoliar, O. and Nam, Y.K.: Transcriptional alteration of two metallothionein isoforms in mud loach (Misgurnus mizolepis) fry during acute heavy metal exposure. Fish. Aquat. Sci., 13:112-117, 2010.
  13. Li, T., Hu, J., Thomas, J.A. and Li, L.: Differential induction of apoptosis by LPS and taxol in monocytic cells. Mol. Immunol., 42:1049-1055, 2005. https://doi.org/10.1016/j.molimm.2004.09.032
  14. Manchado, M., Infante, C., Asensio, E. and Canavate, J.P.: Differential gene expression and dependence on thyroid hormones of two glyceraldehyde-3- phosphate dehydrogenases in the flatfish Senegalese sole (Solea senegalensis Kaup). Gene, 400:1-8, 2007. https://doi.org/10.1016/j.gene.2007.05.008
  15. Mazzola, J.L. and Sirover, M.A.: Subcellular localization of human glyceraldehyde-3-phosphate dehydrogenase is independent of its glycolytic function. Biochim. Biophys. Acta. Gen. Subj., 1622:50-56, 2003. https://doi.org/10.1016/S0304-4165(03)00117-X
  16. Mezquita, J., Pau, M. and Mezquita, C.: Several novel transcripts of glyceraldehyde-3-phosphate dehydrogenase expressed in adult chicken testis. J. Cell. Biochem., 71:127-139, 1998. https://doi.org/10.1002/(SICI)1097-4644(19981001)71:1<127::AID-JCB13>3.0.CO;2-K
  17. Mitter, K., Kotoulas, G., Magoulas, A., Mulero, V., Sepulcre, P., Figueras, A., Novoa, B. and Sarropoulou, E.: Evaluation of candidate reference genes for QPCR during ontogenesis and of immune-relevant tissues of European seabass (Dicentrarchus labrax). Comp. Biochem. Physiol. Biochem., 153B:340-347, 2009.
  18. Murray, P.J.: The JAK-STAT signaling pathway: Input and output integration. J. Immunol., 178:2623-2629, 2007. https://doi.org/10.4049/jimmunol.178.5.2623
  19. Rebl, A., Goldammer, T. and Seyfert, H.M.: Toll-like receptor signaling in bony fish. Vet. Immunol. Immunopathol., 134:139-150, 2010. https://doi.org/10.1016/j.vetimm.2009.09.021
  20. Robbins, A.R., Ward, R.D. and Oliver, C.: A mutation in glyceraldehyde 3-phosphate dehydrogenase alters endocytosis in CHO cells. J. Cell Biol., 130:1093-1104, 1995. https://doi.org/10.1083/jcb.130.5.1093
  21. Schmittgen, T.D. and Livak, K.J.: Analyzing real-time PCR data by the comparative CT method. Nat. Protoc., 3:1101-1108, 2008. https://doi.org/10.1038/nprot.2008.73
  22. Sehgal, P.B.: Paradigm shifts in the cell biology of STAT signaling. Semin. Cell Dev. Biol., 19:329-340, 2008. https://doi.org/10.1016/j.semcdb.2008.07.003
  23. Singh, R. and Green, M.R.: Sequence-specific binding of transfer RNA by glyceraldehyde-3-phosphate dehydrogenase. Science, 259:365-368, 1993. https://doi.org/10.1126/science.8420004
  24. Sirover, M.A.: New nuclear functions of the glycolytic protein, glyceraldehyde-3-phosphate dehydrogenase, in mammalian cells. J. Cell. Biochem., 95:45-52, 2005. https://doi.org/10.1002/jcb.20399
  25. Tang, R., Dodd, A., Lai, D., McNabb, W.C. and Love, D.R.: Validation of zebrafish (Danio rerio) reference genes for quantitative real-time RT-PCR normalization. Acta Biochim. Biophys. Sin., 39:384-390, 2007. https://doi.org/10.1111/j.1745-7270.2007.00283.x
  26. Valavanidis. A., Vlahogianni, T., Dassenakis, M. and Scoullos, M.: Molecular biomarkers of oxidative stress in aquatic organisms in relation to toxic environmental pollutants. Ecotoxicol. Environ. Saf., 64:178-189, 2006. https://doi.org/10.1016/j.ecoenv.2005.03.013
  27. Welch, J.E., Barbee, R.R., Magyar, P.L., Bunch, D.O. and O'Brien, D.A.: Expression of the spermatogenic cell-specific glyceraldehyde 3-phosphate dehydrogenase (GAPDS) in rat testis. Mol. Reprod. Dev., 73:1052-1060, 2006. https://doi.org/10.1002/mrd.20235
  28. Welch, J.E., Brown, P.L., O'Brien, D.A., Magyar, P.L., Bunch, D.O., Mori, C. and Eddy, E.M.: Human glyceraldehyde 3-phosphate dehydrogenase-2 gene is expressed specifically in spermatogenic cells. J. Androl., 21:328-338, 2000.

Cited by

  1. Genomic Organization, Tissue Distribution and Developmental Expression of Glyceraldehyde 3-Phosphate Dehydrogenase Isoforms in Mud Loach Misgurnus mizolepis vol.16, pp.4, 2013, https://doi.org/10.5657/FAS.2013.0291
  2. Evaluation of reference genes for RT-qPCR study in abalone Haliotis discus hannai during heavy metal overload stress vol.19, pp.1, 2016, https://doi.org/10.1186/s41240-016-0022-z